Structures determined by X-ray crystallography are preferred over NMR structures.

Cluster ID / Name

The internal number of the sequence cluster used for unique identification.

Structural variation in clusters

The identification of similar sequences in this report is based on clustering as described here.

The PDBFlex database explores the intrinsic flexibility of protein structures by analyzing structural variations of the same protein across the archive. This allows for the easy identification of regions and types of structural flexibility present in a protein of interest. Structures of protein chains with identical sequences (sequence identity > 95%) are aligned, superimposed and clustered.

Instructions

In the table for each entity, view a list of similar sequences by selecting the link associated with
the percentage cutoff.

CHYMOTRYPSINOGEN NUMBERING (RATHER THAN SEQUENTIAL) SYSTEM IS USED, BASED ON THE TOPOLOGICAL ALIGNMENT WITH THE STRUCTURE OF CHYMOTRYPSINOGEN (H.BRANDSTETTER ET AL., 1992, J.MOL.BIOL., V. 226, 1085). THE N-TERMINUS OF THE FIBRINOPEPTIDE IS ACETYLATED. FIBRINOPEPTIDE SEQUENCE NUMBERS ARE ACE 6 TO ARG 19. A NEW RESIDUE, OPR, HAS BEEN DEFINED FOR THE ARG/GLY COMBINATION IN WHICH THE AMIDE NITROGEN HAS BEEN REPLACED WITH A CH2, MAKING THE NORMAL AMIDE BOND BETWEEN THESE TWO RESIDUES A KETONE BOND. THE FIBRINOPEPTIDE NUMBERING IS CONSEQUENTLY INCREMENTED BY 1 AFTER THIS RESIDUE IN KEEPING WITH THE FIBRINOGEN NUMBERING SCHEME. THERE ARE ALTERNATE CONFORMATIONS FOR RESIDUES PRO 18 AND ARG 19 IN FIBRINOPEPTIDE III.